Abstract
The conjugation of benzoyl-CoA with the aliphatic and acidic amino acids by glycine N-acyltransferase, as well as the amides of the latter group, was investigated. Bovine and human liver benzoyl-amino acid conjugation were investigated using electrospray ionization tandem mass spectrometry (ESI-MS-MS). Bovine glycine N-acyltransferase catalyzed conjugation of benzoyl-CoA with Gly (KmGly = 6.2 mM), Asn (KmAsn = 129 mM), Gln (KmGln = 353 mM), Ala (KmAla = 1573 mM), Glu (KmGlu = 1148 mM) as well as Ser in a sequential mechanism. In the case of the human form, conjugation with Gly (KmGly = 6.4 mM), Ala (KmAla = 997 mM), and Glu was detected. The presence of these alternative conjugates did not inhibit bovine glycine N-acyltransferase activity significantly. Considering the relatively low levels at which these conjugates are formed, it is unlikely that they will have a significant contribution to acyl-amino acid conjugation under normal conditions in vivo. However, their cumulative contribution to acyl-amino acid conjugation under metabolic disease states may prove to have a useful contribution to detoxification of elevated acyl-CoAs. © 2000 John Wiley & Sons, Inc. J Biochem Toxicol 14: 102–109, 2000
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